RDRP_BPSP
ID RDRP_BPSP Reviewed; 576 AA.
AC P09675;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=RNA-directed RNA polymerase subunit beta;
DE EC=2.7.7.48 {ECO:0000250|UniProtKB:P14647};
DE AltName: Full=RNA replicase beta chain;
OS Enterobacteria phage SP (Bacteriophage SP).
OC Viruses; Riboviria; Orthornavirae; Lenarviricota; Leviviricetes;
OC Levivirales; Leviviridae; Allolevivirus.
OX NCBI_TaxID=12027;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3399390; DOI=10.1093/nar/16.13.6205;
RA Hirashima A., Hirose T., Inayama S., Inokuchi Y., Jacobson A.B.;
RT "Analysis of the complete nucleotide sequence of the group IV RNA coliphage
RT SP.";
RL Nucleic Acids Res. 16:6205-6221(1988).
CC -!- FUNCTION: This is the catalytic subunit of the viral RNA-dependent RNA
CC polymerase complex. This complex is involved in viral RNA replication
CC that produces (+)-stranded genomes via a complementary, (-)-stranded
CC intermediate. Binds RNA cooperatively with the host ribosomal protein
CC S1. {ECO:0000250|UniProtKB:P14647}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000250|UniProtKB:P14647,
CC ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P14647};
CC Note=Binds 2 Mg(2+) per subunit, Ca(2+) is used in crystallization to
CC prevent RNA polymerase activity. {ECO:0000250|UniProtKB:P14647};
CC -!- SUBUNIT: Homodimer; the replicase complex can dimerize. Part of the
CC viral RNA-dependent RNA polymerase complex, the other subunits are the
CC host ribosomal protein S1, EF-Tu and EF-Ts. S1 is needed for the
CC initiation of genomic RNA (+)-strand replication.
CC {ECO:0000250|UniProtKB:P14647}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X07489; CAA30375.1; -; mRNA.
DR PIR; S01965; S01965.
DR SMR; P09675; -.
DR PRIDE; P09675; -.
DR Proteomes; UP000000728; Genome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR007096; RNA-dir_Rpol_phage_catalytic.
DR InterPro; IPR005093; RNArep_beta.
DR Pfam; PF03431; RNA_replicase_B; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50522; RDRP_PHAGE; 1.
PE 2: Evidence at transcript level;
KW Magnesium; Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication.
FT CHAIN 1..576
FT /note="RNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000164856"
FT DOMAIN 259..391
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14647"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14647"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14647"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14647"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14647"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14647"
SQ SEQUENCE 576 AA; 65398 MW; EAB30613C21C5F6C CRC64;
MPKTASRRRE ITQLLGKVDI NFEDDIHMSI ANDLFEAYGI PKLDSAEECI NTAFPSLDQG
VDTFRVEYLR AEILSKFDGH PLGIDTEAAA WEKFLAAEEG CRQTNERLSL VKYHDNSILS
WGERVIHTAR RKILKLIGES VPFGDVALRC RFSGGATTSV NRLHGHPSWK HACPQDVTKR
AFKYLQAFKR ACGDVVDLRV NEVRTSNKAV TVPKNSKTDR CIAIEPGWNM FFQLGVGAVL
RDRLRLWKID LNDQSTNQRL ARDGSLLNHL ATIDLSAASD SISLKLVELL MPPEWYDLLT
DLRSDEGILP DGRVVTYEKI SSMGNGYTFE LESLIFAAIA RSVCELLEID QSTVSVYGDD
IIIDTRAAAP LMDVFEYVGF TPNRKKTFCD GPFRESCGKH WFQGVDVTPF YIRRPIRCLA
DMILVLNSIY RWGTVDGIWD PRALTVYEKY LKLLPRNWRR NRIPDGYGDG ALVGLATTNP
FVIVKNYSRL YPVLVEVQRD VKRSEEGSYL YALLRDRETR YSPFLRDADR TGFDEAPLAT
SLRRKTGRYK VAWIQDSAFI RPPYLITGIP EVKLAS